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HEADER HYDROLASE 22-MAY-19 6RT8
TITLE STRUCTURE OF CATHARANTHINE SYNTHASE - AN ALPHA-BETA HYDROLASE FROM
TITLE 2 CATHARANTHUS ROSEUS WITH A CLEAVIMINIUM INTERMEDIATE BOUND
CAVEAT 6RT8 KJE A 401 HAS WRONG CHIRALITY AT ATOM C8 KJE B 401 HAS WRONG
CAVEAT 2 6RT8 CHIRALITY AT ATOM C8 KJE C 401 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 6RT8 C8 KJE D 401 HAS WRONG CHIRALITY AT ATOM C8 KJE E 401 HAS
CAVEAT 4 6RT8 WRONG CHIRALITY AT ATOM C8 KJE F 401 HAS WRONG CHIRALITY AT
CAVEAT 5 6RT8 ATOM C8 KJE G 401 HAS WRONG CHIRALITY AT ATOM C8 KJE H 401
CAVEAT 6 6RT8 HAS WRONG CHIRALITY AT ATOM C8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHARANTHINE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: HYDROLASE 1,CRHL1;
COMPND 5 EC: 4.-.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CATHARANTHUS ROSEUS;
SOURCE 3 ORGANISM_COMMON: MADAGASCAR PERIWINKLE;
SOURCE 4 ORGANISM_TAXID: 4058;
SOURCE 5 GENE: CS, HL1, CAROS025416;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: SOLUBL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: POPINF
KEYWDS ALKALOID, CATHARANTHINE, NATURAL PRODUCT, BIOSYNTHESIS, ALPHA/BETA
KEYWDS 2 HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.CAPUTI,J.FRANKE,K.BUSSEY,S.C.FARROW,I.J.CURCINO VIEIRA,
AUTHOR 2 C.E.M.STEVENSON,D.M.LAWSON,S.E.O'CONNOR
REVDAT 1 04-MAR-20 6RT8 0
JRNL AUTH L.CAPUTI,J.FRANKE,K.BUSSEY,S.C.FARROW,I.J.C.VIEIRA,
JRNL AUTH 2 C.E.M.STEVENSON,D.M.LAWSON,S.E.O'CONNOR
JRNL TITL STRUCTURAL BASIS OF CYCLOADDITION IN BIOSYNTHESIS OF IBOGA
JRNL TITL 2 AND ASPIDOSPERMA ALKALOIDS.
JRNL REF NAT.CHEM.BIOL. 2020
JRNL REFN ESSN 1552-4469
JRNL PMID 32066966
JRNL DOI 10.1038/S41589-019-0460-X
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 145106
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7594
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10578
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.4080
REMARK 3 BIN FREE R VALUE SET COUNT : 588
REMARK 3 BIN FREE R VALUE : 0.3900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19468
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 276
REMARK 3 SOLVENT ATOMS : 388
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.78000
REMARK 3 B22 (A**2) : 0.88000
REMARK 3 B33 (A**2) : -0.94000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.80000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.243
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.228
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.651
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20341 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 18236 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27773 ; 1.522 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 42165 ; 1.269 ; 1.575
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2483 ; 7.215 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 945 ;31.655 ;22.582
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2945 ;14.221 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 76 ;20.943 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2653 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22813 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4411 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 28
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 9 327 B 9 327 10407 0.050 0.050
REMARK 3 2 A 9 327 C 9 327 10493 0.040 0.050
REMARK 3 3 A 9 327 D 9 327 10479 0.040 0.050
REMARK 3 4 A 9 326 E 9 326 9755 0.060 0.050
REMARK 3 5 A 9 327 F 9 327 10357 0.040 0.050
REMARK 3 6 A 9 327 G 9 327 10503 0.040 0.050
REMARK 3 7 A 10 326 H 10 326 10235 0.050 0.050
REMARK 3 8 B 9 327 C 9 327 10422 0.060 0.050
REMARK 3 9 B 9 327 D 9 327 10426 0.050 0.050
REMARK 3 10 B 9 326 E 9 326 9815 0.040 0.050
REMARK 3 11 B 9 327 F 9 327 10265 0.050 0.050
REMARK 3 12 B 9 327 G 9 327 10434 0.040 0.050
REMARK 3 13 B 10 326 H 10 326 10234 0.050 0.050
REMARK 3 14 C 9 327 D 9 327 10468 0.050 0.050
REMARK 3 15 C 9 326 E 9 326 9758 0.060 0.050
REMARK 3 16 C 9 327 F 9 327 10359 0.050 0.050
REMARK 3 17 C 9 327 G 9 327 10499 0.050 0.050
REMARK 3 18 C 10 326 H 10 326 10255 0.050 0.050
REMARK 3 19 D 9 326 E 9 326 9744 0.060 0.050
REMARK 3 20 D 9 327 F 9 327 10349 0.040 0.050
REMARK 3 21 D 9 327 G 9 327 10512 0.030 0.050
REMARK 3 22 D 10 326 H 10 326 10294 0.040 0.050
REMARK 3 23 E 9 326 F 9 326 9732 0.050 0.050
REMARK 3 24 E 9 326 G 9 326 9761 0.050 0.050
REMARK 3 25 E 10 326 H 10 326 9632 0.050 0.050
REMARK 3 26 F 9 327 G 9 327 10388 0.040 0.050
REMARK 3 27 F 10 326 H 10 326 10102 0.040 0.050
REMARK 3 28 G 10 326 H 10 326 10271 0.040 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): 81.9742 -9.7566 18.9403
REMARK 3 T TENSOR
REMARK 3 T11: 0.0962 T22: 0.1066
REMARK 3 T33: 0.1068 T12: 0.0473
REMARK 3 T13: 0.0958 T23: 0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 1.6503 L22: 1.1178
REMARK 3 L33: 2.3728 L12: -0.3113
REMARK 3 L13: -0.0283 L23: -0.1171
REMARK 3 S TENSOR
REMARK 3 S11: 0.1230 S12: -0.0524 S13: 0.1205
REMARK 3 S21: 0.0770 S22: 0.0419 S23: 0.0185
REMARK 3 S31: -0.2314 S32: -0.1320 S33: -0.1649
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 9 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 74.1860 -13.0321 -18.0666
REMARK 3 T TENSOR
REMARK 3 T11: 0.0404 T22: 0.2825
REMARK 3 T33: 0.1139 T12: 0.0860
REMARK 3 T13: 0.0590 T23: 0.1639
REMARK 3 L TENSOR
REMARK 3 L11: 2.2994 L22: 1.4933
REMARK 3 L33: 2.6992 L12: 0.3109
REMARK 3 L13: 0.3325 L23: 0.1416
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: 0.0566 S13: -0.1098
REMARK 3 S21: -0.0396 S22: 0.2020 S23: 0.1087
REMARK 3 S31: -0.0606 S32: -0.3454 S33: -0.1807
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 9 C 401
REMARK 3 ORIGIN FOR THE GROUP (A): 64.7312 -4.9775 104.1061
REMARK 3 T TENSOR
REMARK 3 T11: 0.0815 T22: 0.1701
REMARK 3 T33: 0.0582 T12: 0.0167
REMARK 3 T13: 0.0373 T23: 0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 2.3368 L22: 2.0218
REMARK 3 L33: 2.0880 L12: 0.5694
REMARK 3 L13: -0.6902 L23: -0.0691
REMARK 3 S TENSOR
REMARK 3 S11: -0.0670 S12: 0.0238 S13: -0.1711
REMARK 3 S21: -0.1511 S22: 0.0737 S23: 0.1170
REMARK 3 S31: 0.0605 S32: -0.2026 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 9 D 401
REMARK 3 ORIGIN FOR THE GROUP (A): 88.9907 20.2914 88.8966
REMARK 3 T TENSOR
REMARK 3 T11: 0.1190 T22: 0.1571
REMARK 3 T33: 0.0619 T12: 0.0008
REMARK 3 T13: 0.0697 T23: -0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 1.7496 L22: 3.1653
REMARK 3 L33: 1.8942 L12: 0.2459
REMARK 3 L13: -0.6801 L23: -0.3432
REMARK 3 S TENSOR
REMARK 3 S11: 0.0502 S12: -0.0356 S13: 0.1197
REMARK 3 S21: -0.1542 S22: -0.0115 S23: -0.0758
REMARK 3 S31: -0.1771 S32: -0.0017 S33: -0.0387
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 9 E 401
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1073 11.7596 10.9934
REMARK 3 T TENSOR
REMARK 3 T11: 0.0394 T22: 0.4692
REMARK 3 T33: 0.3880 T12: 0.0110
REMARK 3 T13: 0.0495 T23: 0.3286
REMARK 3 L TENSOR
REMARK 3 L11: 4.9709 L22: 1.5954
REMARK 3 L33: 2.8568 L12: 0.2462
REMARK 3 L13: -0.7429 L23: 0.3737
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: -1.3348 S13: -0.7515
REMARK 3 S21: 0.1816 S22: -0.1953 S23: -0.1561
REMARK 3 S31: 0.2047 S32: 0.0549 S33: 0.2380
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 9 F 401
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8892 21.5430 -24.2025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0437 T22: 0.2445
REMARK 3 T33: 0.1704 T12: -0.0592
REMARK 3 T13: 0.0351 T23: -0.1240
REMARK 3 L TENSOR
REMARK 3 L11: 4.0097 L22: 2.1300
REMARK 3 L33: 1.7328 L12: 1.4138
REMARK 3 L13: -0.9154 L23: -0.4955
REMARK 3 S TENSOR
REMARK 3 S11: -0.3454 S12: 0.8395 S13: -0.4088
REMARK 3 S21: -0.2296 S22: 0.2416 S23: 0.0376
REMARK 3 S31: 0.0213 S32: -0.2438 S33: 0.1038
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 9 G 401
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1917 21.9510 64.3078
REMARK 3 T TENSOR
REMARK 3 T11: 0.2428 T22: 0.1716
REMARK 3 T33: 0.1722 T12: 0.0051
REMARK 3 T13: 0.1783 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 2.1070 L22: 1.8118
REMARK 3 L33: 1.9828 L12: -0.3883
REMARK 3 L13: -0.5911 L23: 0.1906
REMARK 3 S TENSOR
REMARK 3 S11: 0.2214 S12: 0.0218 S13: 0.3384
REMARK 3 S21: -0.0197 S22: -0.1286 S23: 0.0755
REMARK 3 S31: -0.3057 S32: -0.0402 S33: -0.0928
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 9 H 401
REMARK 3 ORIGIN FOR THE GROUP (A): 64.0120 -0.3622 50.8484
REMARK 3 T TENSOR
REMARK 3 T11: 0.1909 T22: 0.2400
REMARK 3 T33: 0.0989 T12: -0.0035
REMARK 3 T13: 0.0632 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 2.9767 L22: 3.1705
REMARK 3 L33: 2.7280 L12: -0.7752
REMARK 3 L13: -1.4780 L23: -0.1004
REMARK 3 S TENSOR
REMARK 3 S11: 0.1209 S12: -0.3355 S13: 0.0995
REMARK 3 S21: 0.1758 S22: -0.0170 S23: -0.4060
REMARK 3 S31: -0.1592 S32: 0.4310 S33: -0.1040
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6RT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102511.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20161101
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 152727
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 52.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 1.12900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.7.17
REMARK 200 STARTING MODEL: 6RS4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL, PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 60.51500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 0
REMARK 465 PRO A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 THR A 7
REMARK 465 SER A 8
REMARK 465 ASN A 144
REMARK 465 SER A 145
REMARK 465 GLY A 146
REMARK 465 LEU A 147
REMARK 465 LYS A 148
REMARK 465 HIS A 328
REMARK 465 GLU A 329
REMARK 465 GLY B 0
REMARK 465 PRO B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 THR B 5
REMARK 465 PRO B 6
REMARK 465 THR B 7
REMARK 465 SER B 8
REMARK 465 ASN B 144
REMARK 465 SER B 145
REMARK 465 GLY B 146
REMARK 465 LEU B 147
REMARK 465 LYS B 148
REMARK 465 HIS B 328
REMARK 465 GLU B 329
REMARK 465 GLY C 0
REMARK 465 PRO C 1
REMARK 465 ALA C 2
REMARK 465 SER C 3
REMARK 465 GLN C 4
REMARK 465 THR C 5
REMARK 465 PRO C 6
REMARK 465 THR C 7
REMARK 465 SER C 8
REMARK 465 ASN C 144
REMARK 465 SER C 145
REMARK 465 GLY C 146
REMARK 465 LEU C 147
REMARK 465 LYS C 148
REMARK 465 HIS C 328
REMARK 465 GLU C 329
REMARK 465 GLY D 0
REMARK 465 PRO D 1
REMARK 465 ALA D 2
REMARK 465 SER D 3
REMARK 465 GLN D 4
REMARK 465 THR D 5
REMARK 465 PRO D 6
REMARK 465 THR D 7
REMARK 465 SER D 8
REMARK 465 ASN D 144
REMARK 465 SER D 145
REMARK 465 GLY D 146
REMARK 465 LEU D 147
REMARK 465 LYS D 148
REMARK 465 HIS D 328
REMARK 465 GLU D 329
REMARK 465 GLY E 0
REMARK 465 PRO E 1
REMARK 465 ALA E 2
REMARK 465 SER E 3
REMARK 465 GLN E 4
REMARK 465 THR E 5
REMARK 465 PRO E 6
REMARK 465 THR E 7
REMARK 465 SER E 8
REMARK 465 ILE E 67
REMARK 465 SER E 68
REMARK 465 ASP E 69
REMARK 465 HIS E 70
REMARK 465 ASN E 144
REMARK 465 SER E 145
REMARK 465 GLY E 146
REMARK 465 LEU E 147
REMARK 465 LYS E 148
REMARK 465 PRO E 209
REMARK 465 THR E 210
REMARK 465 SER E 211
REMARK 465 THR E 212
REMARK 465 LYS E 327
REMARK 465 HIS E 328
REMARK 465 GLU E 329
REMARK 465 GLY F 0
REMARK 465 PRO F 1
REMARK 465 ALA F 2
REMARK 465 SER F 3
REMARK 465 GLN F 4
REMARK 465 THR F 5
REMARK 465 PRO F 6
REMARK 465 THR F 7
REMARK 465 SER F 8
REMARK 465 ASN F 144
REMARK 465 SER F 145
REMARK 465 GLY F 146
REMARK 465 LEU F 147
REMARK 465 LYS F 148
REMARK 465 THR F 149
REMARK 465 HIS F 328
REMARK 465 GLU F 329
REMARK 465 GLY G 0
REMARK 465 PRO G 1
REMARK 465 ALA G 2
REMARK 465 SER G 3
REMARK 465 GLN G 4
REMARK 465 THR G 5
REMARK 465 PRO G 6
REMARK 465 THR G 7
REMARK 465 SER G 8
REMARK 465 ASN G 144
REMARK 465 SER G 145
REMARK 465 GLY G 146
REMARK 465 LEU G 147
REMARK 465 LYS G 148
REMARK 465 THR G 149
REMARK 465 HIS G 328
REMARK 465 GLU G 329
REMARK 465 GLY H 0
REMARK 465 PRO H 1
REMARK 465 ALA H 2
REMARK 465 SER H 3
REMARK 465 GLN H 4
REMARK 465 THR H 5
REMARK 465 PRO H 6
REMARK 465 THR H 7
REMARK 465 SER H 8
REMARK 465 ASP H 9
REMARK 465 ASN H 144
REMARK 465 SER H 145
REMARK 465 GLY H 146
REMARK 465 LEU H 147
REMARK 465 LYS H 148
REMARK 465 GLU H 329
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 23 CD CE NZ
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 ASP A 69 CG OD1 OD2
REMARK 470 HIS A 70 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 71 CG CD OE1 OE2
REMARK 470 LYS A 106 CD CE NZ
REMARK 470 THR A 149 OG1 CG2
REMARK 470 LYS A 187 CD CE NZ
REMARK 470 LYS A 195 CE NZ
REMARK 470 ASN A 248 CG OD1 ND2
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 GLU A 284 CG CD OE1 OE2
REMARK 470 GLU A 287 CG CD OE1 OE2
REMARK 470 LYS A 288 CE NZ
REMARK 470 ASP B 9 CG OD1 OD2
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 LYS B 66 CD CE NZ
REMARK 470 ASP B 69 CG OD1 OD2
REMARK 470 HIS B 70 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 149 OG1 CG2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 LYS B 213 CG CD CE NZ
REMARK 470 GLU B 247 CG CD OE1 OE2
REMARK 470 LYS B 276 CG CD CE NZ
REMARK 470 GLU B 284 CG CD OE1 OE2
REMARK 470 GLU B 287 CG CD OE1 OE2
REMARK 470 LYS B 288 CG CD CE NZ
REMARK 470 LYS B 292 CE NZ
REMARK 470 ASP C 9 CG OD1 OD2
REMARK 470 GLU C 10 CG CD OE1 OE2
REMARK 470 LYS C 23 CD CE NZ
REMARK 470 LYS C 66 CE NZ
REMARK 470 SER C 68 OG
REMARK 470 ASP C 69 CG OD1 OD2
REMARK 470 HIS C 70 CG ND1 CD2 CE1 NE2
REMARK 470 THR C 149 OG1 CG2
REMARK 470 LYS C 187 CD CE NZ
REMARK 470 LYS C 195 CE NZ
REMARK 470 THR C 212 OG1 CG2
REMARK 470 LYS C 213 CG CD CE NZ
REMARK 470 LYS C 276 CE NZ
REMARK 470 GLU C 287 CD OE1 OE2
REMARK 470 LYS C 288 CE NZ
REMARK 470 LYS C 292 CE NZ
REMARK 470 GLU D 10 CG CD OE1 OE2
REMARK 470 LYS D 23 CG CD CE NZ
REMARK 470 LEU D 30 CG CD1 CD2
REMARK 470 LYS D 66 CD CE NZ
REMARK 470 SER D 68 OG
REMARK 470 ASP D 69 CG OD1 OD2
REMARK 470 HIS D 70 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 106 CE NZ
REMARK 470 THR D 149 OG1 CG2
REMARK 470 LYS D 195 CE NZ
REMARK 470 GLU D 247 CG CD OE1 OE2
REMARK 470 ASN D 248 CG OD1 ND2
REMARK 470 LYS D 276 CG CD CE NZ
REMARK 470 GLU D 284 CG CD OE1 OE2
REMARK 470 LYS D 292 CE NZ
REMARK 470 GLU E 10 CG CD OE1 OE2
REMARK 470 LYS E 66 CG CD CE NZ
REMARK 470 GLU E 71 CG CD OE1 OE2
REMARK 470 LYS E 72 CG CD CE NZ
REMARK 470 LYS E 106 CE NZ
REMARK 470 ASP E 143 CG OD1 OD2
REMARK 470 THR E 149 OG1 CG2
REMARK 470 LYS E 187 CG CD CE NZ
REMARK 470 LYS E 189 CG CD CE NZ
REMARK 470 LYS E 195 CG CD CE NZ
REMARK 470 LEU E 197 CG CD1 CD2
REMARK 470 LEU E 201 CG CD1 CD2
REMARK 470 LYS E 213 CG CD CE NZ
REMARK 470 LEU E 214 CG CD1 CD2
REMARK 470 GLU E 219 CG CD OE1 OE2
REMARK 470 GLU E 247 CG CD OE1 OE2
REMARK 470 ASN E 248 CG OD1 ND2
REMARK 470 ARG E 259 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 264 CG CD1 CD2
REMARK 470 LYS E 276 CG CD CE NZ
REMARK 470 ASP E 277 CG OD1 OD2
REMARK 470 ASN E 279 CG OD1 ND2
REMARK 470 ILE E 283 CG1 CG2 CD1
REMARK 470 GLU E 284 CG CD OE1 OE2
REMARK 470 LEU E 286 CG CD1 CD2
REMARK 470 GLU E 287 CG CD OE1 OE2
REMARK 470 LYS E 288 CE NZ
REMARK 470 TRP E 291 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP E 291 CZ3 CH2
REMARK 470 LYS E 292 CG CD CE NZ
REMARK 470 GLU E 294 CG CD OE1 OE2
REMARK 470 ASN E 317 CG OD1 ND2
REMARK 470 ARG E 321 CG CD NE CZ NH1 NH2
REMARK 470 PHE E 325 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS F 23 CG CD CE NZ
REMARK 470 LYS F 66 CG CD CE NZ
REMARK 470 ILE F 67 CG1 CG2 CD1
REMARK 470 ASP F 69 CG OD1 OD2
REMARK 470 HIS F 70 CG ND1 CD2 CE1 NE2
REMARK 470 GLU F 71 CG CD OE1 OE2
REMARK 470 ASP F 143 CG OD1 OD2
REMARK 470 LYS F 153 CD CE NZ
REMARK 470 LYS F 187 CG CD CE NZ
REMARK 470 LYS F 189 CG CD CE NZ
REMARK 470 LYS F 195 CG CD CE NZ
REMARK 470 LYS F 213 CE NZ
REMARK 470 ARG F 259 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 276 CD CE NZ
REMARK 470 LYS F 288 CE NZ
REMARK 470 LYS F 292 CG CD CE NZ
REMARK 470 GLU F 294 CG CD OE1 OE2
REMARK 470 LYS G 23 CD CE NZ
REMARK 470 LYS G 66 CD CE NZ
REMARK 470 SER G 68 OG
REMARK 470 ASP G 69 CG OD1 OD2
REMARK 470 HIS G 70 CG ND1 CD2 CE1 NE2
REMARK 470 GLU G 71 CG CD OE1 OE2
REMARK 470 LYS G 187 CE NZ
REMARK 470 LYS G 195 CE NZ
REMARK 470 LYS G 213 CG CD CE NZ
REMARK 470 ASN G 232 CG OD1 ND2
REMARK 470 GLU G 247 CG CD OE1 OE2
REMARK 470 LYS G 276 CG CD CE NZ
REMARK 470 GLU G 284 CD OE1 OE2
REMARK 470 LYS G 288 CE NZ
REMARK 470 LYS G 292 CE NZ
REMARK 470 GLU H 10 CG CD OE1 OE2
REMARK 470 ILE H 12 CG1 CG2 CD1
REMARK 470 LYS H 23 CG CD CE NZ
REMARK 470 ARG H 26 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 28 CG CD OE1 OE2
REMARK 470 LEU H 30 CG CD1 CD2
REMARK 470 HIS H 31 CG ND1 CD2 CE1 NE2
REMARK 470 ASP H 69 CG OD1 OD2
REMARK 470 HIS H 70 CG ND1 CD2 CE1 NE2
REMARK 470 GLU H 71 CG CD OE1 OE2
REMARK 470 LYS H 106 CG CD CE NZ
REMARK 470 THR H 149 OG1 CG2
REMARK 470 LYS H 189 CG CD CE NZ
REMARK 470 LYS H 195 CE NZ
REMARK 470 SER H 211 OG
REMARK 470 THR H 212 OG1 CG2
REMARK 470 LYS H 213 CG CD CE NZ
REMARK 470 ASN H 232 CG OD1 ND2
REMARK 470 GLU H 247 CG CD OE1 OE2
REMARK 470 ASN H 248 CG OD1 ND2
REMARK 470 LYS H 276 CG CD CE NZ
REMARK 470 GLU H 284 CG CD OE1 OE2
REMARK 470 GLU H 287 CG CD OE1 OE2
REMARK 470 LYS H 288 CD CE NZ
REMARK 470 HIS H 328 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 66 126.78 -37.37
REMARK 500 SER A 68 -73.31 -103.58
REMARK 500 ALA A 82 72.88 88.17
REMARK 500 GLU A 87 -168.56 63.53
REMARK 500 SER A 88 147.24 -170.47
REMARK 500 ALA A 150 155.96 -49.71
REMARK 500 SER A 172 -135.58 44.98
REMARK 500 LYS A 189 160.10 75.70
REMARK 500 TYR A 203 76.92 57.63
REMARK 500 TYR A 255 123.52 -39.41
REMARK 500 SER A 269 -118.63 52.18
REMARK 500 HIS B 31 56.15 -98.26
REMARK 500 LYS B 66 127.11 -38.66
REMARK 500 SER B 68 -72.50 -104.58
REMARK 500 ALA B 82 70.35 84.87
REMARK 500 GLU B 87 -168.58 63.32
REMARK 500 SER B 88 149.52 -170.21
REMARK 500 SER B 172 -136.02 45.00
REMARK 500 LYS B 189 158.86 74.77
REMARK 500 TYR B 203 77.70 56.84
REMARK 500 TYR B 255 123.31 -37.81
REMARK 500 SER B 269 -118.70 52.20
REMARK 500 SER C 68 -71.70 -104.74
REMARK 500 ALA C 82 71.81 85.90
REMARK 500 GLU C 87 -169.18 63.63
REMARK 500 SER C 88 148.01 -170.83
REMARK 500 SER C 172 -136.01 45.40
REMARK 500 LYS C 189 156.79 75.39
REMARK 500 TYR C 203 77.20 57.55
REMARK 500 TYR C 255 122.88 -37.61
REMARK 500 SER C 269 -118.13 52.14
REMARK 500 SER D 68 -73.39 -103.42
REMARK 500 ALA D 82 70.23 82.83
REMARK 500 GLU D 87 -168.36 63.02
REMARK 500 SER D 88 148.52 -171.23
REMARK 500 SER D 172 -135.68 45.13
REMARK 500 LYS D 189 157.00 74.98
REMARK 500 TYR D 203 78.70 55.95
REMARK 500 TYR D 255 122.78 -38.53
REMARK 500 SER D 269 -119.04 52.00
REMARK 500 SER E 16 131.66 -38.55
REMARK 500 HIS E 31 47.17 -98.44
REMARK 500 ALA E 82 71.97 83.22
REMARK 500 GLU E 87 -168.34 61.96
REMARK 500 SER E 88 148.02 -170.78
REMARK 500 SER E 172 -136.39 44.86
REMARK 500 LYS E 189 157.13 74.74
REMARK 500 TYR E 203 77.64 57.52
REMARK 500 TYR E 255 122.31 -37.06
REMARK 500 SER E 269 -118.27 52.67
REMARK 500
REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJE C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJE D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJE E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJE F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJE G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJE H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G H 402
DBREF1 6RT8 A 6 329 UNP CS_CATRO
DBREF2 6RT8 A A0A2P1GIW2 7 330
DBREF1 6RT8 B 6 329 UNP CS_CATRO
DBREF2 6RT8 B A0A2P1GIW2 7 330
DBREF1 6RT8 C 6 329 UNP CS_CATRO
DBREF2 6RT8 C A0A2P1GIW2 7 330
DBREF1 6RT8 D 6 329 UNP CS_CATRO
DBREF2 6RT8 D A0A2P1GIW2 7 330
DBREF1 6RT8 E 6 329 UNP CS_CATRO
DBREF2 6RT8 E A0A2P1GIW2 7 330
DBREF1 6RT8 F 6 329 UNP CS_CATRO
DBREF2 6RT8 F A0A2P1GIW2 7 330
DBREF1 6RT8 G 6 329 UNP CS_CATRO
DBREF2 6RT8 G A0A2P1GIW2 7 330
DBREF1 6RT8 H 6 329 UNP CS_CATRO
DBREF2 6RT8 H A0A2P1GIW2 7 330
SEQADV 6RT8 GLY A 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 PRO A 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 ALA A 2 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 SER A 3 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLN A 4 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 THR A 5 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLY B 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 PRO B 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 ALA B 2 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 SER B 3 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLN B 4 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 THR B 5 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLY C 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 PRO C 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 ALA C 2 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 SER C 3 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLN C 4 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 THR C 5 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLY D 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 PRO D 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 ALA D 2 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 SER D 3 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLN D 4 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 THR D 5 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLY E 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 PRO E 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 ALA E 2 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 SER E 3 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLN E 4 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 THR E 5 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLY F 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 PRO F 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 ALA F 2 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 SER F 3 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLN F 4 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 THR F 5 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLY G 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 PRO G 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 ALA G 2 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 SER G 3 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLN G 4 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 THR G 5 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLY H 0 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 PRO H 1 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 ALA H 2 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 SER H 3 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 GLN H 4 UNP A0A2P1GIW EXPRESSION TAG
SEQADV 6RT8 THR H 5 UNP A0A2P1GIW EXPRESSION TAG
SEQRES 1 A 330 GLY PRO ALA SER GLN THR PRO THR SER ASP GLU THR ILE
SEQRES 2 A 330 TRP ASP LEU SER PRO TYR ILE LYS ILE PHE LYS ASP GLY
SEQRES 3 A 330 ARG VAL GLU ARG LEU HIS ASN SER PRO TYR VAL PRO PRO
SEQRES 4 A 330 SER LEU ASN ASP PRO GLU THR GLY VAL SER TRP LYS ASP
SEQRES 5 A 330 VAL PRO ILE SER SER GLN VAL SER ALA ARG VAL TYR ILE
SEQRES 6 A 330 PRO LYS ILE SER ASP HIS GLU LYS LEU PRO ILE PHE VAL
SEQRES 7 A 330 TYR VAL HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE
SEQRES 8 A 330 ARG SER PHE PHE HIS THR PHE VAL LYS HIS PHE VAL ALA
SEQRES 9 A 330 GLU THR LYS VAL ILE GLY VAL SER ILE GLU TYR ARG LEU
SEQRES 10 A 330 ALA PRO GLU HIS LEU LEU PRO ALA ALA TYR GLU ASP CYS
SEQRES 11 A 330 TRP GLU ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU
SEQRES 12 A 330 ASP ASN SER GLY LEU LYS THR ALA ILE ASP LYS ASP PRO
SEQRES 13 A 330 TRP ILE ILE ASN TYR GLY ASP PHE ASP ARG LEU TYR LEU
SEQRES 14 A 330 ALA GLY ASP SER PRO GLY ALA ASN ILE VAL HIS ASN THR
SEQRES 15 A 330 LEU ILE ARG ALA GLY LYS GLU LYS LEU LYS GLY GLY VAL
SEQRES 16 A 330 LYS ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE ILE
SEQRES 17 A 330 ILE PRO THR SER THR LYS LEU SER ASP ASP PHE GLU TYR
SEQRES 18 A 330 ASN TYR THR CYS TYR TRP LYS LEU ALA TYR PRO ASN ALA
SEQRES 19 A 330 PRO GLY GLY MET ASN ASN PRO MET ILE ASN PRO ILE ALA
SEQRES 20 A 330 GLU ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG
SEQRES 21 A 330 LEU LEU VAL THR LEU VAL SER MET ILE SER THR THR PRO
SEQRES 22 A 330 ASP GLU THR LYS ASP ILE ASN ALA VAL TYR ILE GLU ALA
SEQRES 23 A 330 LEU GLU LYS SER GLY TRP LYS GLY GLU LEU GLU VAL ALA
SEQRES 24 A 330 ASP PHE ASP ALA ASP TYR PHE GLU LEU PHE THR LEU GLU
SEQRES 25 A 330 THR GLU MET GLY LYS ASN MET PHE ARG ARG LEU ALA SER
SEQRES 26 A 330 PHE ILE LYS HIS GLU
SEQRES 1 B 330 GLY PRO ALA SER GLN THR PRO THR SER ASP GLU THR ILE
SEQRES 2 B 330 TRP ASP LEU SER PRO TYR ILE LYS ILE PHE LYS ASP GLY
SEQRES 3 B 330 ARG VAL GLU ARG LEU HIS ASN SER PRO TYR VAL PRO PRO
SEQRES 4 B 330 SER LEU ASN ASP PRO GLU THR GLY VAL SER TRP LYS ASP
SEQRES 5 B 330 VAL PRO ILE SER SER GLN VAL SER ALA ARG VAL TYR ILE
SEQRES 6 B 330 PRO LYS ILE SER ASP HIS GLU LYS LEU PRO ILE PHE VAL
SEQRES 7 B 330 TYR VAL HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE
SEQRES 8 B 330 ARG SER PHE PHE HIS THR PHE VAL LYS HIS PHE VAL ALA
SEQRES 9 B 330 GLU THR LYS VAL ILE GLY VAL SER ILE GLU TYR ARG LEU
SEQRES 10 B 330 ALA PRO GLU HIS LEU LEU PRO ALA ALA TYR GLU ASP CYS
SEQRES 11 B 330 TRP GLU ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU
SEQRES 12 B 330 ASP ASN SER GLY LEU LYS THR ALA ILE ASP LYS ASP PRO
SEQRES 13 B 330 TRP ILE ILE ASN TYR GLY ASP PHE ASP ARG LEU TYR LEU
SEQRES 14 B 330 ALA GLY ASP SER PRO GLY ALA ASN ILE VAL HIS ASN THR
SEQRES 15 B 330 LEU ILE ARG ALA GLY LYS GLU LYS LEU LYS GLY GLY VAL
SEQRES 16 B 330 LYS ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE ILE
SEQRES 17 B 330 ILE PRO THR SER THR LYS LEU SER ASP ASP PHE GLU TYR
SEQRES 18 B 330 ASN TYR THR CYS TYR TRP LYS LEU ALA TYR PRO ASN ALA
SEQRES 19 B 330 PRO GLY GLY MET ASN ASN PRO MET ILE ASN PRO ILE ALA
SEQRES 20 B 330 GLU ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG
SEQRES 21 B 330 LEU LEU VAL THR LEU VAL SER MET ILE SER THR THR PRO
SEQRES 22 B 330 ASP GLU THR LYS ASP ILE ASN ALA VAL TYR ILE GLU ALA
SEQRES 23 B 330 LEU GLU LYS SER GLY TRP LYS GLY GLU LEU GLU VAL ALA
SEQRES 24 B 330 ASP PHE ASP ALA ASP TYR PHE GLU LEU PHE THR LEU GLU
SEQRES 25 B 330 THR GLU MET GLY LYS ASN MET PHE ARG ARG LEU ALA SER
SEQRES 26 B 330 PHE ILE LYS HIS GLU
SEQRES 1 C 330 GLY PRO ALA SER GLN THR PRO THR SER ASP GLU THR ILE
SEQRES 2 C 330 TRP ASP LEU SER PRO TYR ILE LYS ILE PHE LYS ASP GLY
SEQRES 3 C 330 ARG VAL GLU ARG LEU HIS ASN SER PRO TYR VAL PRO PRO
SEQRES 4 C 330 SER LEU ASN ASP PRO GLU THR GLY VAL SER TRP LYS ASP
SEQRES 5 C 330 VAL PRO ILE SER SER GLN VAL SER ALA ARG VAL TYR ILE
SEQRES 6 C 330 PRO LYS ILE SER ASP HIS GLU LYS LEU PRO ILE PHE VAL
SEQRES 7 C 330 TYR VAL HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE
SEQRES 8 C 330 ARG SER PHE PHE HIS THR PHE VAL LYS HIS PHE VAL ALA
SEQRES 9 C 330 GLU THR LYS VAL ILE GLY VAL SER ILE GLU TYR ARG LEU
SEQRES 10 C 330 ALA PRO GLU HIS LEU LEU PRO ALA ALA TYR GLU ASP CYS
SEQRES 11 C 330 TRP GLU ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU
SEQRES 12 C 330 ASP ASN SER GLY LEU LYS THR ALA ILE ASP LYS ASP PRO
SEQRES 13 C 330 TRP ILE ILE ASN TYR GLY ASP PHE ASP ARG LEU TYR LEU
SEQRES 14 C 330 ALA GLY ASP SER PRO GLY ALA ASN ILE VAL HIS ASN THR
SEQRES 15 C 330 LEU ILE ARG ALA GLY LYS GLU LYS LEU LYS GLY GLY VAL
SEQRES 16 C 330 LYS ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE ILE
SEQRES 17 C 330 ILE PRO THR SER THR LYS LEU SER ASP ASP PHE GLU TYR
SEQRES 18 C 330 ASN TYR THR CYS TYR TRP LYS LEU ALA TYR PRO ASN ALA
SEQRES 19 C 330 PRO GLY GLY MET ASN ASN PRO MET ILE ASN PRO ILE ALA
SEQRES 20 C 330 GLU ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG
SEQRES 21 C 330 LEU LEU VAL THR LEU VAL SER MET ILE SER THR THR PRO
SEQRES 22 C 330 ASP GLU THR LYS ASP ILE ASN ALA VAL TYR ILE GLU ALA
SEQRES 23 C 330 LEU GLU LYS SER GLY TRP LYS GLY GLU LEU GLU VAL ALA
SEQRES 24 C 330 ASP PHE ASP ALA ASP TYR PHE GLU LEU PHE THR LEU GLU
SEQRES 25 C 330 THR GLU MET GLY LYS ASN MET PHE ARG ARG LEU ALA SER
SEQRES 26 C 330 PHE ILE LYS HIS GLU
SEQRES 1 D 330 GLY PRO ALA SER GLN THR PRO THR SER ASP GLU THR ILE
SEQRES 2 D 330 TRP ASP LEU SER PRO TYR ILE LYS ILE PHE LYS ASP GLY
SEQRES 3 D 330 ARG VAL GLU ARG LEU HIS ASN SER PRO TYR VAL PRO PRO
SEQRES 4 D 330 SER LEU ASN ASP PRO GLU THR GLY VAL SER TRP LYS ASP
SEQRES 5 D 330 VAL PRO ILE SER SER GLN VAL SER ALA ARG VAL TYR ILE
SEQRES 6 D 330 PRO LYS ILE SER ASP HIS GLU LYS LEU PRO ILE PHE VAL
SEQRES 7 D 330 TYR VAL HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE
SEQRES 8 D 330 ARG SER PHE PHE HIS THR PHE VAL LYS HIS PHE VAL ALA
SEQRES 9 D 330 GLU THR LYS VAL ILE GLY VAL SER ILE GLU TYR ARG LEU
SEQRES 10 D 330 ALA PRO GLU HIS LEU LEU PRO ALA ALA TYR GLU ASP CYS
SEQRES 11 D 330 TRP GLU ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU
SEQRES 12 D 330 ASP ASN SER GLY LEU LYS THR ALA ILE ASP LYS ASP PRO
SEQRES 13 D 330 TRP ILE ILE ASN TYR GLY ASP PHE ASP ARG LEU TYR LEU
SEQRES 14 D 330 ALA GLY ASP SER PRO GLY ALA ASN ILE VAL HIS ASN THR
SEQRES 15 D 330 LEU ILE ARG ALA GLY LYS GLU LYS LEU LYS GLY GLY VAL
SEQRES 16 D 330 LYS ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE ILE
SEQRES 17 D 330 ILE PRO THR SER THR LYS LEU SER ASP ASP PHE GLU TYR
SEQRES 18 D 330 ASN TYR THR CYS TYR TRP LYS LEU ALA TYR PRO ASN ALA
SEQRES 19 D 330 PRO GLY GLY MET ASN ASN PRO MET ILE ASN PRO ILE ALA
SEQRES 20 D 330 GLU ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG
SEQRES 21 D 330 LEU LEU VAL THR LEU VAL SER MET ILE SER THR THR PRO
SEQRES 22 D 330 ASP GLU THR LYS ASP ILE ASN ALA VAL TYR ILE GLU ALA
SEQRES 23 D 330 LEU GLU LYS SER GLY TRP LYS GLY GLU LEU GLU VAL ALA
SEQRES 24 D 330 ASP PHE ASP ALA ASP TYR PHE GLU LEU PHE THR LEU GLU
SEQRES 25 D 330 THR GLU MET GLY LYS ASN MET PHE ARG ARG LEU ALA SER
SEQRES 26 D 330 PHE ILE LYS HIS GLU
SEQRES 1 E 330 GLY PRO ALA SER GLN THR PRO THR SER ASP GLU THR ILE
SEQRES 2 E 330 TRP ASP LEU SER PRO TYR ILE LYS ILE PHE LYS ASP GLY
SEQRES 3 E 330 ARG VAL GLU ARG LEU HIS ASN SER PRO TYR VAL PRO PRO
SEQRES 4 E 330 SER LEU ASN ASP PRO GLU THR GLY VAL SER TRP LYS ASP
SEQRES 5 E 330 VAL PRO ILE SER SER GLN VAL SER ALA ARG VAL TYR ILE
SEQRES 6 E 330 PRO LYS ILE SER ASP HIS GLU LYS LEU PRO ILE PHE VAL
SEQRES 7 E 330 TYR VAL HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE
SEQRES 8 E 330 ARG SER PHE PHE HIS THR PHE VAL LYS HIS PHE VAL ALA
SEQRES 9 E 330 GLU THR LYS VAL ILE GLY VAL SER ILE GLU TYR ARG LEU
SEQRES 10 E 330 ALA PRO GLU HIS LEU LEU PRO ALA ALA TYR GLU ASP CYS
SEQRES 11 E 330 TRP GLU ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU
SEQRES 12 E 330 ASP ASN SER GLY LEU LYS THR ALA ILE ASP LYS ASP PRO
SEQRES 13 E 330 TRP ILE ILE ASN TYR GLY ASP PHE ASP ARG LEU TYR LEU
SEQRES 14 E 330 ALA GLY ASP SER PRO GLY ALA ASN ILE VAL HIS ASN THR
SEQRES 15 E 330 LEU ILE ARG ALA GLY LYS GLU LYS LEU LYS GLY GLY VAL
SEQRES 16 E 330 LYS ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE ILE
SEQRES 17 E 330 ILE PRO THR SER THR LYS LEU SER ASP ASP PHE GLU TYR
SEQRES 18 E 330 ASN TYR THR CYS TYR TRP LYS LEU ALA TYR PRO ASN ALA
SEQRES 19 E 330 PRO GLY GLY MET ASN ASN PRO MET ILE ASN PRO ILE ALA
SEQRES 20 E 330 GLU ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG
SEQRES 21 E 330 LEU LEU VAL THR LEU VAL SER MET ILE SER THR THR PRO
SEQRES 22 E 330 ASP GLU THR LYS ASP ILE ASN ALA VAL TYR ILE GLU ALA
SEQRES 23 E 330 LEU GLU LYS SER GLY TRP LYS GLY GLU LEU GLU VAL ALA
SEQRES 24 E 330 ASP PHE ASP ALA ASP TYR PHE GLU LEU PHE THR LEU GLU
SEQRES 25 E 330 THR GLU MET GLY LYS ASN MET PHE ARG ARG LEU ALA SER
SEQRES 26 E 330 PHE ILE LYS HIS GLU
SEQRES 1 F 330 GLY PRO ALA SER GLN THR PRO THR SER ASP GLU THR ILE
SEQRES 2 F 330 TRP ASP LEU SER PRO TYR ILE LYS ILE PHE LYS ASP GLY
SEQRES 3 F 330 ARG VAL GLU ARG LEU HIS ASN SER PRO TYR VAL PRO PRO
SEQRES 4 F 330 SER LEU ASN ASP PRO GLU THR GLY VAL SER TRP LYS ASP
SEQRES 5 F 330 VAL PRO ILE SER SER GLN VAL SER ALA ARG VAL TYR ILE
SEQRES 6 F 330 PRO LYS ILE SER ASP HIS GLU LYS LEU PRO ILE PHE VAL
SEQRES 7 F 330 TYR VAL HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE
SEQRES 8 F 330 ARG SER PHE PHE HIS THR PHE VAL LYS HIS PHE VAL ALA
SEQRES 9 F 330 GLU THR LYS VAL ILE GLY VAL SER ILE GLU TYR ARG LEU
SEQRES 10 F 330 ALA PRO GLU HIS LEU LEU PRO ALA ALA TYR GLU ASP CYS
SEQRES 11 F 330 TRP GLU ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU
SEQRES 12 F 330 ASP ASN SER GLY LEU LYS THR ALA ILE ASP LYS ASP PRO
SEQRES 13 F 330 TRP ILE ILE ASN TYR GLY ASP PHE ASP ARG LEU TYR LEU
SEQRES 14 F 330 ALA GLY ASP SER PRO GLY ALA ASN ILE VAL HIS ASN THR
SEQRES 15 F 330 LEU ILE ARG ALA GLY LYS GLU LYS LEU LYS GLY GLY VAL
SEQRES 16 F 330 LYS ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE ILE
SEQRES 17 F 330 ILE PRO THR SER THR LYS LEU SER ASP ASP PHE GLU TYR
SEQRES 18 F 330 ASN TYR THR CYS TYR TRP LYS LEU ALA TYR PRO ASN ALA
SEQRES 19 F 330 PRO GLY GLY MET ASN ASN PRO MET ILE ASN PRO ILE ALA
SEQRES 20 F 330 GLU ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG
SEQRES 21 F 330 LEU LEU VAL THR LEU VAL SER MET ILE SER THR THR PRO
SEQRES 22 F 330 ASP GLU THR LYS ASP ILE ASN ALA VAL TYR ILE GLU ALA
SEQRES 23 F 330 LEU GLU LYS SER GLY TRP LYS GLY GLU LEU GLU VAL ALA
SEQRES 24 F 330 ASP PHE ASP ALA ASP TYR PHE GLU LEU PHE THR LEU GLU
SEQRES 25 F 330 THR GLU MET GLY LYS ASN MET PHE ARG ARG LEU ALA SER
SEQRES 26 F 330 PHE ILE LYS HIS GLU
SEQRES 1 G 330 GLY PRO ALA SER GLN THR PRO THR SER ASP GLU THR ILE
SEQRES 2 G 330 TRP ASP LEU SER PRO TYR ILE LYS ILE PHE LYS ASP GLY
SEQRES 3 G 330 ARG VAL GLU ARG LEU HIS ASN SER PRO TYR VAL PRO PRO
SEQRES 4 G 330 SER LEU ASN ASP PRO GLU THR GLY VAL SER TRP LYS ASP
SEQRES 5 G 330 VAL PRO ILE SER SER GLN VAL SER ALA ARG VAL TYR ILE
SEQRES 6 G 330 PRO LYS ILE SER ASP HIS GLU LYS LEU PRO ILE PHE VAL
SEQRES 7 G 330 TYR VAL HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE
SEQRES 8 G 330 ARG SER PHE PHE HIS THR PHE VAL LYS HIS PHE VAL ALA
SEQRES 9 G 330 GLU THR LYS VAL ILE GLY VAL SER ILE GLU TYR ARG LEU
SEQRES 10 G 330 ALA PRO GLU HIS LEU LEU PRO ALA ALA TYR GLU ASP CYS
SEQRES 11 G 330 TRP GLU ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU
SEQRES 12 G 330 ASP ASN SER GLY LEU LYS THR ALA ILE ASP LYS ASP PRO
SEQRES 13 G 330 TRP ILE ILE ASN TYR GLY ASP PHE ASP ARG LEU TYR LEU
SEQRES 14 G 330 ALA GLY ASP SER PRO GLY ALA ASN ILE VAL HIS ASN THR
SEQRES 15 G 330 LEU ILE ARG ALA GLY LYS GLU LYS LEU LYS GLY GLY VAL
SEQRES 16 G 330 LYS ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE ILE
SEQRES 17 G 330 ILE PRO THR SER THR LYS LEU SER ASP ASP PHE GLU TYR
SEQRES 18 G 330 ASN TYR THR CYS TYR TRP LYS LEU ALA TYR PRO ASN ALA
SEQRES 19 G 330 PRO GLY GLY MET ASN ASN PRO MET ILE ASN PRO ILE ALA
SEQRES 20 G 330 GLU ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG
SEQRES 21 G 330 LEU LEU VAL THR LEU VAL SER MET ILE SER THR THR PRO
SEQRES 22 G 330 ASP GLU THR LYS ASP ILE ASN ALA VAL TYR ILE GLU ALA
SEQRES 23 G 330 LEU GLU LYS SER GLY TRP LYS GLY GLU LEU GLU VAL ALA
SEQRES 24 G 330 ASP PHE ASP ALA ASP TYR PHE GLU LEU PHE THR LEU GLU
SEQRES 25 G 330 THR GLU MET GLY LYS ASN MET PHE ARG ARG LEU ALA SER
SEQRES 26 G 330 PHE ILE LYS HIS GLU
SEQRES 1 H 330 GLY PRO ALA SER GLN THR PRO THR SER ASP GLU THR ILE
SEQRES 2 H 330 TRP ASP LEU SER PRO TYR ILE LYS ILE PHE LYS ASP GLY
SEQRES 3 H 330 ARG VAL GLU ARG LEU HIS ASN SER PRO TYR VAL PRO PRO
SEQRES 4 H 330 SER LEU ASN ASP PRO GLU THR GLY VAL SER TRP LYS ASP
SEQRES 5 H 330 VAL PRO ILE SER SER GLN VAL SER ALA ARG VAL TYR ILE
SEQRES 6 H 330 PRO LYS ILE SER ASP HIS GLU LYS LEU PRO ILE PHE VAL
SEQRES 7 H 330 TYR VAL HIS GLY ALA GLY PHE CYS LEU GLU SER ALA PHE
SEQRES 8 H 330 ARG SER PHE PHE HIS THR PHE VAL LYS HIS PHE VAL ALA
SEQRES 9 H 330 GLU THR LYS VAL ILE GLY VAL SER ILE GLU TYR ARG LEU
SEQRES 10 H 330 ALA PRO GLU HIS LEU LEU PRO ALA ALA TYR GLU ASP CYS
SEQRES 11 H 330 TRP GLU ALA LEU GLN TRP VAL ALA SER HIS VAL GLY LEU
SEQRES 12 H 330 ASP ASN SER GLY LEU LYS THR ALA ILE ASP LYS ASP PRO
SEQRES 13 H 330 TRP ILE ILE ASN TYR GLY ASP PHE ASP ARG LEU TYR LEU
SEQRES 14 H 330 ALA GLY ASP SER PRO GLY ALA ASN ILE VAL HIS ASN THR
SEQRES 15 H 330 LEU ILE ARG ALA GLY LYS GLU LYS LEU LYS GLY GLY VAL
SEQRES 16 H 330 LYS ILE LEU GLY ALA ILE LEU TYR TYR PRO TYR PHE ILE
SEQRES 17 H 330 ILE PRO THR SER THR LYS LEU SER ASP ASP PHE GLU TYR
SEQRES 18 H 330 ASN TYR THR CYS TYR TRP LYS LEU ALA TYR PRO ASN ALA
SEQRES 19 H 330 PRO GLY GLY MET ASN ASN PRO MET ILE ASN PRO ILE ALA
SEQRES 20 H 330 GLU ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS SER ARG
SEQRES 21 H 330 LEU LEU VAL THR LEU VAL SER MET ILE SER THR THR PRO
SEQRES 22 H 330 ASP GLU THR LYS ASP ILE ASN ALA VAL TYR ILE GLU ALA
SEQRES 23 H 330 LEU GLU LYS SER GLY TRP LYS GLY GLU LEU GLU VAL ALA
SEQRES 24 H 330 ASP PHE ASP ALA ASP TYR PHE GLU LEU PHE THR LEU GLU
SEQRES 25 H 330 THR GLU MET GLY LYS ASN MET PHE ARG ARG LEU ALA SER
SEQRES 26 H 330 PHE ILE LYS HIS GLU
HET KJE A 401 25
HET P6G A 402 19
HET KJE B 401 25
HET KJE C 401 25
HET P6G C 402 19
HET KJE D 401 25
HET KJE E 401 25
HET P6G E 402 19
HET KJE F 401 25
HET KJE G 401 25
HET KJE H 401 25
HET P6G H 402 19
HETNAM KJE 18-CARBOXYMETHOXY-CLEAVIMINIUM
HETNAM P6G HEXAETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 9 KJE 8(C21 H25 N2 O2 1+)
FORMUL 10 P6G 4(C12 H26 O7)
FORMUL 21 HOH *388(H2 O)
HELIX 1 AA1 ARG A 91 LYS A 106 1 16
HELIX 2 AA2 PRO A 123 SER A 138 1 16
HELIX 3 AA3 ASP A 154 TYR A 160 1 7
HELIX 4 AA4 SER A 172 LYS A 189 1 18
HELIX 5 AA5 LEU A 190 VAL A 194 5 5
HELIX 6 AA6 SER A 215 TYR A 230 1 16
HELIX 7 AA7 GLY A 235 ASN A 239 5 5
HELIX 8 AA8 ASP A 251 TYR A 255 5 5
HELIX 9 AA9 THR A 275 SER A 289 1 15
HELIX 10 AB1 PHE A 305 LEU A 310 1 6
HELIX 11 AB2 THR A 312 ILE A 326 1 15
HELIX 12 AB3 ARG B 91 LYS B 106 1 16
HELIX 13 AB4 PRO B 123 SER B 138 1 16
HELIX 14 AB5 ASP B 154 TYR B 160 1 7
HELIX 15 AB6 SER B 172 LYS B 189 1 18
HELIX 16 AB7 LEU B 190 VAL B 194 5 5
HELIX 17 AB8 SER B 215 TYR B 230 1 16
HELIX 18 AB9 GLY B 235 ASN B 239 5 5
HELIX 19 AC1 ASP B 251 TYR B 255 5 5
HELIX 20 AC2 THR B 275 LYS B 288 1 14
HELIX 21 AC3 PHE B 305 LEU B 310 1 6
HELIX 22 AC4 THR B 312 ILE B 326 1 15
HELIX 23 AC5 ARG C 91 LYS C 106 1 16
HELIX 24 AC6 PRO C 123 SER C 138 1 16
HELIX 25 AC7 ASP C 154 TYR C 160 1 7
HELIX 26 AC8 SER C 172 LYS C 189 1 18
HELIX 27 AC9 LEU C 190 VAL C 194 5 5
HELIX 28 AD1 SER C 215 TYR C 230 1 16
HELIX 29 AD2 GLY C 235 ASN C 239 5 5
HELIX 30 AD3 ASP C 251 TYR C 255 5 5
HELIX 31 AD4 THR C 275 SER C 289 1 15
HELIX 32 AD5 PHE C 305 LEU C 310 1 6
HELIX 33 AD6 THR C 312 ILE C 326 1 15
HELIX 34 AD7 ARG D 91 LYS D 106 1 16
HELIX 35 AD8 PRO D 123 SER D 138 1 16
HELIX 36 AD9 ASP D 154 TYR D 160 1 7
HELIX 37 AE1 SER D 172 LYS D 189 1 18
HELIX 38 AE2 LEU D 190 VAL D 194 5 5
HELIX 39 AE3 SER D 215 TYR D 230 1 16
HELIX 40 AE4 GLY D 235 ASN D 239 5 5
HELIX 41 AE5 ASP D 251 TYR D 255 5 5
HELIX 42 AE6 THR D 275 SER D 289 1 15
HELIX 43 AE7 PHE D 305 LEU D 310 1 6
HELIX 44 AE8 THR D 312 ILE D 326 1 15
HELIX 45 AE9 ARG E 91 LYS E 106 1 16
HELIX 46 AF1 PRO E 123 SER E 138 1 16
HELIX 47 AF2 ASP E 154 TYR E 160 1 7
HELIX 48 AF3 SER E 172 LYS E 189 1 18
HELIX 49 AF4 LEU E 190 VAL E 194 5 5
HELIX 50 AF5 SER E 215 TYR E 230 1 16
HELIX 51 AF6 GLY E 235 ASN E 239 5 5
HELIX 52 AF7 ASP E 251 TYR E 255 5 5
HELIX 53 AF8 THR E 275 SER E 289 1 15
HELIX 54 AF9 PHE E 305 LEU E 310 1 6
HELIX 55 AG1 THR E 312 ILE E 326 1 15
HELIX 56 AG2 ARG F 91 LYS F 106 1 16
HELIX 57 AG3 PRO F 123 SER F 138 1 16
HELIX 58 AG4 ASP F 154 TYR F 160 1 7
HELIX 59 AG5 SER F 172 LYS F 189 1 18
HELIX 60 AG6 LEU F 190 VAL F 194 5 5
HELIX 61 AG7 SER F 215 TYR F 230 1 16
HELIX 62 AG8 GLY F 235 ASN F 239 5 5
HELIX 63 AG9 ASP F 251 TYR F 255 5 5
HELIX 64 AH1 THR F 275 SER F 289 1 15
HELIX 65 AH2 PHE F 305 LEU F 310 1 6
HELIX 66 AH3 THR F 312 ILE F 326 1 15
HELIX 67 AH4 ARG G 91 LYS G 106 1 16
HELIX 68 AH5 PRO G 123 SER G 138 1 16
HELIX 69 AH6 ASP G 154 TYR G 160 1 7
HELIX 70 AH7 SER G 172 LYS G 189 1 18
HELIX 71 AH8 LEU G 190 VAL G 194 5 5
HELIX 72 AH9 SER G 215 TYR G 230 1 16
HELIX 73 AI1 GLY G 235 ASN G 239 5 5
HELIX 74 AI2 ASP G 251 TYR G 255 5 5
HELIX 75 AI3 THR G 275 SER G 289 1 15
HELIX 76 AI4 PHE G 305 LEU G 310 1 6
HELIX 77 AI5 THR G 312 ILE G 326 1 15
HELIX 78 AI6 ARG H 91 LYS H 106 1 16
HELIX 79 AI7 PRO H 123 SER H 138 1 16
HELIX 80 AI8 ASP H 154 TYR H 160 1 7
HELIX 81 AI9 SER H 172 GLU H 188 1 17
HELIX 82 AJ1 LEU H 190 VAL H 194 5 5
HELIX 83 AJ2 SER H 215 TYR H 230 1 16
HELIX 84 AJ3 GLY H 235 ASN H 239 5 5
HELIX 85 AJ4 ASP H 251 TYR H 255 5 5
HELIX 86 AJ5 THR H 275 SER H 289 1 15
HELIX 87 AJ6 PHE H 305 LEU H 310 1 6
HELIX 88 AJ7 THR H 312 ILE H 326 1 15
SHEET 1 AA1 3 THR A 11 LEU A 15 0
SHEET 2 AA1 3 ILE A 19 PHE A 22 -1 O ILE A 21 N TRP A 13
SHEET 3 AA1 3 VAL A 27 ARG A 29 -1 O GLU A 28 N LYS A 20
SHEET 1 AA216 SER A 48 PRO A 53 0
SHEET 2 AA216 SER A 59 ILE A 64 -1 O VAL A 62 N LYS A 50
SHEET 3 AA216 ILE A 108 GLU A 113 -1 O GLU A 113 N SER A 59
SHEET 4 AA216 LEU A 73 VAL A 79 1 N PHE A 76 O ILE A 108
SHEET 5 AA216 GLY A 161 ASP A 171 1 O TYR A 167 N ILE A 75
SHEET 6 AA216 GLY A 198 TYR A 202 1 O TYR A 202 N GLY A 170
SHEET 7 AA216 ARG A 259 LEU A 264 1 O THR A 263 N LEU A 201
SHEET 8 AA216 GLU A 294 ASP A 299 1 O GLU A 296 N LEU A 260
SHEET 9 AA216 GLU H 294 ASP H 299 -1 O ASP H 299 N LEU A 295
SHEET 10 AA216 CYS H 257 LEU H 264 1 N LEU H 260 O GLU H 296
SHEET 11 AA216 ILE H 196 TYR H 202 1 N LEU H 201 O THR H 263
SHEET 12 AA216 GLY H 161 ASP H 171 1 N GLY H 170 O TYR H 202
SHEET 13 AA216 LEU H 73 VAL H 79 1 N ILE H 75 O TYR H 167
SHEET 14 AA216 ILE H 108 GLU H 113 1 O ILE H 108 N PHE H 76
SHEET 15 AA216 SER H 59 ILE H 64 -1 N ARG H 61 O SER H 111
SHEET 16 AA216 SER H 48 PRO H 53 -1 N LYS H 50 O VAL H 62
SHEET 1 AA3 2 MET A 267 ILE A 268 0
SHEET 2 AA3 2 THR A 271 PRO A 272 -1 O THR A 271 N ILE A 268
SHEET 1 AA4 3 THR B 11 LEU B 15 0
SHEET 2 AA4 3 ILE B 19 PHE B 22 -1 O ILE B 21 N TRP B 13
SHEET 3 AA4 3 VAL B 27 GLU B 28 -1 O GLU B 28 N LYS B 20
SHEET 1 AA5 8 SER B 48 PRO B 53 0
SHEET 2 AA5 8 SER B 59 ILE B 64 -1 O VAL B 62 N LYS B 50
SHEET 3 AA5 8 ILE B 108 GLU B 113 -1 O GLU B 113 N SER B 59
SHEET 4 AA5 8 LEU B 73 VAL B 79 1 N PHE B 76 O ILE B 108
SHEET 5 AA5 8 GLY B 161 ASP B 171 1 O TYR B 167 N ILE B 75
SHEET 6 AA5 8 GLY B 198 TYR B 202 1 O TYR B 202 N GLY B 170
SHEET 7 AA5 8 ARG B 259 LEU B 264 1 O THR B 263 N LEU B 201
SHEET 8 AA5 8 GLU B 294 ASP B 299 1 O GLU B 296 N LEU B 260
SHEET 1 AA6 2 MET B 267 ILE B 268 0
SHEET 2 AA6 2 THR B 271 PRO B 272 -1 O THR B 271 N ILE B 268
SHEET 1 AA7 3 THR C 11 LEU C 15 0
SHEET 2 AA7 3 ILE C 19 PHE C 22 -1 O ILE C 21 N TRP C 13
SHEET 3 AA7 3 VAL C 27 GLU C 28 -1 O GLU C 28 N LYS C 20
SHEET 1 AA8 8 SER C 48 PRO C 53 0
SHEET 2 AA8 8 SER C 59 ILE C 64 -1 O VAL C 62 N LYS C 50
SHEET 3 AA8 8 ILE C 108 GLU C 113 -1 O GLU C 113 N SER C 59
SHEET 4 AA8 8 LEU C 73 VAL C 79 1 N PHE C 76 O ILE C 108
SHEET 5 AA8 8 GLY C 161 ASP C 171 1 O TYR C 167 N ILE C 75
SHEET 6 AA8 8 GLY C 198 TYR C 202 1 O TYR C 202 N GLY C 170
SHEET 7 AA8 8 ARG C 259 LEU C 264 1 O THR C 263 N LEU C 201
SHEET 8 AA8 8 GLU C 294 ASP C 299 1 O GLU C 296 N LEU C 260
SHEET 1 AA9 2 MET C 267 ILE C 268 0
SHEET 2 AA9 2 THR C 271 PRO C 272 -1 O THR C 271 N ILE C 268
SHEET 1 AB1 3 THR D 11 LEU D 15 0
SHEET 2 AB1 3 ILE D 19 PHE D 22 -1 O ILE D 21 N TRP D 13
SHEET 3 AB1 3 VAL D 27 GLU D 28 -1 O GLU D 28 N LYS D 20
SHEET 1 AB2 8 SER D 48 PRO D 53 0
SHEET 2 AB2 8 SER D 59 ILE D 64 -1 O VAL D 62 N LYS D 50
SHEET 3 AB2 8 ILE D 108 GLU D 113 -1 O GLU D 113 N SER D 59
SHEET 4 AB2 8 LEU D 73 VAL D 79 1 N PHE D 76 O ILE D 108
SHEET 5 AB2 8 GLY D 161 ASP D 171 1 O TYR D 167 N ILE D 75
SHEET 6 AB2 8 ILE D 196 TYR D 202 1 O TYR D 202 N GLY D 170
SHEET 7 AB2 8 CYS D 257 LEU D 264 1 O LEU D 261 N ALA D 199
SHEET 8 AB2 8 GLU D 294 ASP D 299 1 O GLU D 296 N LEU D 260
SHEET 1 AB3 2 MET D 267 ILE D 268 0
SHEET 2 AB3 2 THR D 271 PRO D 272 -1 O THR D 271 N ILE D 268
SHEET 1 AB4 3 THR E 11 LEU E 15 0
SHEET 2 AB4 3 ILE E 19 PHE E 22 -1 O ILE E 21 N TRP E 13
SHEET 3 AB4 3 VAL E 27 GLU E 28 -1 O GLU E 28 N LYS E 20
SHEET 1 AB5 8 SER E 48 PRO E 53 0
SHEET 2 AB5 8 SER E 59 ILE E 64 -1 O VAL E 62 N LYS E 50
SHEET 3 AB5 8 ILE E 108 GLU E 113 -1 O GLU E 113 N SER E 59
SHEET 4 AB5 8 LEU E 73 VAL E 79 1 N PHE E 76 O ILE E 108
SHEET 5 AB5 8 GLY E 161 ASP E 171 1 O TYR E 167 N ILE E 75
SHEET 6 AB5 8 ILE E 196 TYR E 202 1 O TYR E 202 N GLY E 170
SHEET 7 AB5 8 CYS E 257 LEU E 264 1 O LEU E 261 N ALA E 199
SHEET 8 AB5 8 GLU E 294 ASP E 299 1 O GLU E 296 N LEU E 260
SHEET 1 AB6 2 MET E 267 ILE E 268 0
SHEET 2 AB6 2 THR E 271 PRO E 272 -1 O THR E 271 N ILE E 268
SHEET 1 AB7 3 THR F 11 LEU F 15 0
SHEET 2 AB7 3 ILE F 19 PHE F 22 -1 O ILE F 21 N TRP F 13
SHEET 3 AB7 3 VAL F 27 GLU F 28 -1 O GLU F 28 N LYS F 20
SHEET 1 AB8 8 SER F 48 PRO F 53 0
SHEET 2 AB8 8 SER F 59 ILE F 64 -1 O VAL F 62 N LYS F 50
SHEET 3 AB8 8 ILE F 108 GLU F 113 -1 O GLU F 113 N SER F 59
SHEET 4 AB8 8 LEU F 73 VAL F 79 1 N PHE F 76 O ILE F 108
SHEET 5 AB8 8 GLY F 161 ASP F 171 1 O TYR F 167 N ILE F 75
SHEET 6 AB8 8 ILE F 196 TYR F 202 1 O TYR F 202 N GLY F 170
SHEET 7 AB8 8 CYS F 257 LEU F 264 1 O LEU F 261 N ALA F 199
SHEET 8 AB8 8 GLU F 294 ASP F 299 1 O GLU F 296 N LEU F 260
SHEET 1 AB9 2 MET F 267 ILE F 268 0
SHEET 2 AB9 2 THR F 271 PRO F 272 -1 O THR F 271 N ILE F 268
SHEET 1 AC1 3 THR G 11 LEU G 15 0
SHEET 2 AC1 3 ILE G 19 PHE G 22 -1 O ILE G 21 N ILE G 12
SHEET 3 AC1 3 VAL G 27 GLU G 28 -1 O GLU G 28 N LYS G 20
SHEET 1 AC2 8 SER G 48 PRO G 53 0
SHEET 2 AC2 8 SER G 59 ILE G 64 -1 O VAL G 62 N LYS G 50
SHEET 3 AC2 8 ILE G 108 GLU G 113 -1 O GLU G 113 N SER G 59
SHEET 4 AC2 8 LEU G 73 VAL G 79 1 N PHE G 76 O ILE G 108
SHEET 5 AC2 8 GLY G 161 ASP G 171 1 O TYR G 167 N ILE G 75
SHEET 6 AC2 8 ILE G 196 TYR G 202 1 O TYR G 202 N GLY G 170
SHEET 7 AC2 8 CYS G 257 LEU G 264 1 O THR G 263 N LEU G 201
SHEET 8 AC2 8 GLU G 294 ASP G 299 1 O GLU G 296 N LEU G 260
SHEET 1 AC3 2 MET G 267 ILE G 268 0
SHEET 2 AC3 2 THR G 271 PRO G 272 -1 O THR G 271 N ILE G 268
SHEET 1 AC4 3 THR H 11 LEU H 15 0
SHEET 2 AC4 3 ILE H 19 PHE H 22 -1 O ILE H 21 N TRP H 13
SHEET 3 AC4 3 VAL H 27 GLU H 28 -1 O GLU H 28 N LYS H 20
SHEET 1 AC5 2 MET H 267 ILE H 268 0
SHEET 2 AC5 2 THR H 271 PRO H 272 -1 O THR H 271 N ILE H 268
CISPEP 1 SER A 16 PRO A 17 0 5.71
CISPEP 2 ALA A 117 PRO A 118 0 -4.69
CISPEP 3 LEU A 122 PRO A 123 0 7.60
CISPEP 4 SER B 16 PRO B 17 0 8.09
CISPEP 5 ALA B 117 PRO B 118 0 -3.31
CISPEP 6 LEU B 122 PRO B 123 0 5.25
CISPEP 7 SER C 16 PRO C 17 0 5.65
CISPEP 8 ALA C 117 PRO C 118 0 -3.87
CISPEP 9 LEU C 122 PRO C 123 0 7.10
CISPEP 10 SER D 16 PRO D 17 0 6.10
CISPEP 11 ALA D 117 PRO D 118 0 -3.32
CISPEP 12 LEU D 122 PRO D 123 0 6.74
CISPEP 13 SER E 16 PRO E 17 0 5.88
CISPEP 14 ALA E 117 PRO E 118 0 -3.37
CISPEP 15 LEU E 122 PRO E 123 0 5.16
CISPEP 16 SER F 16 PRO F 17 0 4.76
CISPEP 17 ALA F 117 PRO F 118 0 -3.32
CISPEP 18 LEU F 122 PRO F 123 0 8.14
CISPEP 19 SER G 16 PRO G 17 0 5.00
CISPEP 20 ALA G 117 PRO G 118 0 -4.33
CISPEP 21 LEU G 122 PRO G 123 0 5.93
CISPEP 22 SER H 16 PRO H 17 0 6.54
CISPEP 23 ALA H 117 PRO H 118 0 -3.99
CISPEP 24 LEU H 122 PRO H 123 0 6.25
SITE 1 AC1 11 TYR A 18 HIS A 31 ALA A 82 GLY A 83
SITE 2 AC1 11 SER A 172 PRO A 173 TYR A 205 ASN A 221
SITE 3 AC1 11 TYR A 225 ILE A 268 TYR A 304
SITE 1 AC2 14 ASN A 32 TYR A 35 SER A 88 ARG A 91
SITE 2 AC2 14 GLU A 113 HOH A 552 HOH A 556 ARG B 29
SITE 3 AC2 14 ASN B 32 TYR B 35 SER B 88 ARG B 91
SITE 4 AC2 14 GLU B 113 LEU B 116
SITE 1 AC3 10 TYR B 18 ALA B 82 GLY B 83 SER B 172
SITE 2 AC3 10 PRO B 173 TYR B 205 ASN B 221 TYR B 225
SITE 3 AC3 10 ILE B 268 TYR B 304
SITE 1 AC4 12 TYR C 18 HIS C 31 ALA C 82 GLY C 83
SITE 2 AC4 12 SER C 172 PRO C 173 TYR C 205 PHE C 218
SITE 3 AC4 12 ASN C 221 TYR C 225 ILE C 268 TYR C 304
SITE 1 AC5 9 ASN C 32 TYR C 35 SER C 88 ARG C 91
SITE 2 AC5 9 GLU C 113 ARG D 29 ASN D 32 TYR D 35
SITE 3 AC5 9 ARG D 91
SITE 1 AC6 13 TYR D 18 HIS D 31 ALA D 82 GLY D 83
SITE 2 AC6 13 PHE D 93 SER D 172 PRO D 173 TYR D 203
SITE 3 AC6 13 TYR D 205 ASN D 221 TYR D 225 ILE D 268
SITE 4 AC6 13 TYR D 304
SITE 1 AC7 11 TYR E 18 ALA E 82 GLY E 83 SER E 172
SITE 2 AC7 11 PRO E 173 TYR E 203 TYR E 205 ASN E 221
SITE 3 AC7 11 TYR E 225 ILE E 268 TYR E 304
SITE 1 AC8 11 ASN E 32 TYR E 35 GLU E 87 SER E 88
SITE 2 AC8 11 ARG E 91 GLU E 113 ASN F 32 TYR F 35
SITE 3 AC8 11 SER F 88 ARG F 91 GLU F 113
SITE 1 AC9 12 TYR F 18 HIS F 31 ALA F 82 GLY F 83
SITE 2 AC9 12 SER F 172 PRO F 173 TYR F 205 PHE F 218
SITE 3 AC9 12 ASN F 221 TYR F 225 ILE F 268 TYR F 304
SITE 1 AD1 12 TYR G 18 HIS G 31 ALA G 82 GLY G 83
SITE 2 AD1 12 PHE G 93 SER G 172 PRO G 173 TYR G 205
SITE 3 AD1 12 ASN G 221 TYR G 225 ILE G 268 TYR G 304
SITE 1 AD2 10 TYR H 18 ALA H 82 GLY H 83 PHE H 93
SITE 2 AD2 10 SER H 172 PRO H 173 TYR H 205 ASN H 221
SITE 3 AD2 10 TYR H 225 TYR H 304
SITE 1 AD3 13 ARG G 29 ASN G 32 TYR G 35 SER G 88
SITE 2 AD3 13 ARG G 91 ARG H 29 ASN H 32 TYR H 35
SITE 3 AD3 13 GLU H 87 SER H 88 ARG H 91 GLU H 113
SITE 4 AD3 13 LEU H 116
CRYST1 81.540 121.030 157.980 90.00 99.02 90.00 P 1 21 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012264 0.000000 0.001947 0.00000
SCALE2 0.000000 0.008262 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006409 0.00000
TER 2462 LYS A 327
TER 4920 LYS B 327
TER 7385 LYS C 327
TER 9847 LYS D 327
TER 12161 ILE E 326
TER 14600 LYS F 327
TER 17056 LYS G 327
TER 19476 HIS H 328
MASTER 861 0 12 88 104 0 39 620132 8 276 208
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